Z-Ala-Ala-Arg-OH | 50465-92-4

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: Z-Ala-Ala-Arg-OH
• 英文别名: N-benzyloxycarbonyl-alanyl-alanyl-arginine；Z-Ala-Ala-Arg；n-Carbobenzoxy-l-alanyl-l-alanyl-l-arginine；(2S)-5-(diaminomethylideneamino)-2-[[(2S)-2-[[(2S)-2-(phenylmethoxycarbonylamino)propanoyl]amino]propanoyl]amino]pentanoic acid
• CAS: 50465-92-4
• 化学式: C₂₀H₃₀N₆O₆
• 分子量: 450.495
• InChiKey: FJHXUUVTVKBIAD-YDHLFZDLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  32
• 可旋转键数：
  13
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.45
• 拓扑面积：
  198
• 氢给体数：
  6
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Z-Ala-Ala-Arg-OH 在 Streptomyces bikiniensis 27 (VKPM Ac-1783) carboxypeptidase 作用下， 生成 L-精氨酸 、 N-(苄氧羰基)-L-丙氨酰-L-丙氨酸
  参考文献：
  名称：

  Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties

  摘要：

  A metallocarboxypeptidase produced by Streptomyces bikiniensis 27 strain (VKPM Ac-1783) (CPSb) was purified and characterized. The enzyme cleaves both basic and hydrophobic C-terminal amino acid residues from synthetic peptides, that is, it possesses specificity of mammalian carboxypeptidases A and B. The enzyme also hydrolyzes peptides bearing glutamic acid at the C-end. CPSb exhibits its maximal activity at pH 7.0-7.6 and 55A degrees C. The nucleotide sequence encoding the mature CPSb in S. bikiniensis 27 (VKPM Ac-1783) genome (Accession No. GU362077) was determined. It is shown that the primary structure of the mature enzyme has a moderate degree of identity with orthologs from Streptomyces griseus (79% identity) and Streptomyces avermitilis (85% identity).

  DOI：

  10.1134/s0006297910080122

文献信息

• Peptide Synthesis in Organic Media with the Use of Subtilisin 72 Immobilized on a Poly(Vinyl Alcohol) Cryogel
  作者：A. V. Belyaeva、A. V. Bacheva、E. S. Oksenoit、E. N. Lysogorskaya、V. I. Lozinskii、I. Yu. Filippova

  DOI：10.1007/s11171-005-0072-y

  日期：2005.11

  Subtilisin 72 serine protease (EC 3.4.21.14) immobilized on a poly(vinyl alcohol) cryogel was used as a catalyst in the syntheses of N-protected peptide p-nitroanilides of the general formulas Z(or Boc)-Xaa-Phe-pNA (Xaa = Leu or Ala), Z-Ala-Xaa-Yaa-pNA (Xaa = Leu or Ala; Yaa = Leu or Phe), and Z-Ala-Ala-Xaa-Yaa-pNA (Xaa = Leu, Arg, or Gly; Yaa = Phe, Leu, Gly, Asp, or Glu). The syntheses were carried out in DMF-acetonitrile mixtures. A number of protected di-, tri-, and tetrapeptides were prepared in yields up to 99%. The syntheses were found to retain stereoselectivity under the conditions studied. The activation of carboxyl group of the acylating component was shown to have a positive effect upon the coupling rate.

  将固定于聚乙烯醇冻胶上的72丝氨酸蛋白酶（EC 3.4.21.14）用作合成N-保护肽对硝基苯胺的催化剂，其通式为Z（或Boc）-Xaa-Phe-pNA（Xaa=亮氨酸或丙氨酸）、Z-Ala-Xaa-Yaa-pNA（Xaa=亮氨酸或丙氨酸；Yaa=亮氨酸或苯丙氨酸）和Z-Ala-Ala-Xaa-Yaa-pNA（Xaa=亮氨酸、精氨酸或甘氨酸；Yaa=苯丙氨酸、亮氨酸、甘氨酸、天冬氨酸或谷氨酸）。合成在DMF-乙腈混合物中进行。制备了一系列二肽、三肽和四肽保护物，收率高达99%。研究发现，在所研究的条件下，合成保留了立体选择性。酰化成分羧基的活化对偶联率有积极影响。
• Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties
  作者：A. V. Serkina、I. A. Zalunin、E. I. Levitin、T. A. Voejkova、B. V. Tyaglov、L. M. Novikova、L. K. Emeljanova、G. E. Konstantinova、G. G. Chestukhina

  DOI：10.1134/s0006297910080122

  日期：2010.8

  A metallocarboxypeptidase produced by Streptomyces bikiniensis 27 strain (VKPM Ac-1783) (CPSb) was purified and characterized. The enzyme cleaves both basic and hydrophobic C-terminal amino acid residues from synthetic peptides, that is, it possesses specificity of mammalian carboxypeptidases A and B. The enzyme also hydrolyzes peptides bearing glutamic acid at the C-end. CPSb exhibits its maximal activity at pH 7.0-7.6 and 55A degrees C. The nucleotide sequence encoding the mature CPSb in S. bikiniensis 27 (VKPM Ac-1783) genome (Accession No. GU362077) was determined. It is shown that the primary structure of the mature enzyme has a moderate degree of identity with orthologs from Streptomyces griseus (79% identity) and Streptomyces avermitilis (85% identity).